ID A0A2T7NFV8_POMCA Unreviewed; 504 AA.
AC A0A2T7NFV8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=C0Q70_20544 {ECO:0000313|EMBL:PVD20050.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD20050.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD20050.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD20050.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD20050.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD20050.1}.
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DR EMBL; PZQS01000013; PVD20050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7NFV8; -.
DR STRING; 400727.A0A2T7NFV8; -.
DR EnsemblMetazoa; XM_025221651.1; XP_025077436.1; LOC112554066.
DR OMA; HRFCMIC; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000245119; Linkage Group LG13.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20343; BRcat_RBR_HHARI-like; 1.
DR CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR CDD; cd16626; RING-HC_RBR_HHARI; 1.
DR FunFam; 1.20.120.1750:FF:000002; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF21235; UBA_ARI1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 128..339
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 132..177
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 59308 MW; FCBE72841A621F00 CRC64;
MDSDGEMVID EAESDDISEE ELPMEMEPAE SSSTHERRDD EDFHYEVLSA DQIVQFMVDS
IKEVNAVVQI PTTITRILLN HFKWDKEKLM ERYYDGDQER LFSEAHVISP HRRDLKPRRS
TRSAPPDERV ECEICCYPVP NTEMTGLECG HKFCAKCWAE YLTSKIIDEG MGQTISCAAF
GCDILVDDAT VMKLLCEPKV KLKYQQIITN SFVECNRLLR WCPAPDCGHA VKVTYYDSKP
VTCVCGHSFC FACGENWHDP VKCIWLKKWI KKCDDDSETS NWIAANTKEC PKCHVTIEKD
GGCNHMVCKN QNCKADFCWV CLGPWEPHGS SWYNCNRYNE DDAKKARDNQ EKSRAALQRY
LFYCNRYMNH MQSLKFEHKL YTAVRSKMEE MQQHNMSWIE VQFLKKAVDV LCMCRQTLMY
TYVFAFYLRK NNQSIIFEDN QKDLENATEQ LSEYLERDIS SDMLQDIKQK VQDKYRYCES
RRKVLLDHVH EGYEKEQWEY QEYL
//
